pyruvate kinase


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Related to pyruvate kinase: pyruvate kinase deficiency

py·ru·vate ki·nase (PK),

phosphoenolpyruvate kinase; a phosphotransferase catalyzing transfer of phosphate from phosphoenolpyruvate to ADP, forming ATP and pyruvate; other nucleoside phosphates can participate in the reaction; a key step in glycolysis; a deficiency in pyruvate kinase will lead to hemolytic anemia.

py·ru·vate ki·nase

(PK) (pī'rū-vāt kī'nās)
A phosphotransferase catalyzing the transfer of phosphate from phosphoenolpyruvate to adenosine diphosphate, forming adenosine triphosphate and pyruvate; other nucleoside phosphates can participate in the reaction; a key step in glycolysis; pyruvate kinase deficiency leads to hemolytic anemia.

py·ru·vate ki·nase

(PK) (pī'rū-vāt kī'nās)
A phosphotransferase catalyzing the transfer of phosphate from phosphoenolpyruvate to adenosine diphosphate, forming adenosine triphosphate and pyruvate; other nucleoside phosphates can participate in the reaction; a key step in glycolysis; pyruvate kinase deficiency leads to hemolytic anemia.
References in periodicals archive ?
Insulinotropic effect of cinnamaldehyde on transcriptional regulation of pyruvate kinase, phosphoenol pyruvate carboxykinase and GLUT4 translocation in experimental diabetic rats.
cDNAof GLUT2 and pyruvate kinase were analyzed using semi-quantitative PCR with Es Taq Mastermix (CoWin) and analyzed by 2% agarose gel electrophoresis and fluorescence gel image analysis using JS-780 Automatic Gel Imager (Shanghai Peiqing Science & Technology, China).
The activities of hexokinase and pyruvate kinase were reduced while the activities of glucose-6-phosphatase and fructosel, 6-bisphosphatase were increased in rats fed high fructose.
The enzyme, pyruvate kinase, comes in two forms, but the research found that one, PKM2, enabled accelerated glucose consumption.
By contrast, lactate is stable because, with enolase inhibited, no phosphoenolpyruvate is formed and thus there is no substrate for pyruvate kinase and there is no production of pyruvate or lactic acid.
They found an enzyme called pyruvate kinase M2 gobbles up glucose to fuel the disease's spread.
Pyruvate kinase (ATP-pyruvate 2-O-phosphotransferase, EC 2.7.1.40, further denoted as PK) catalyses the final step of glycolysis, transferring the phosphoryl group from phosphoenolpyruvate (PEP) to ADP and producing pyruvate and ATP [1]:
Experimental studies have shown that many glycolytic enzymes bind cytoskeletal proteins reversibly including lactate dehydrogenase (LDH), fructose-1,6-bisphosphate aldolase (aldolase), glyceraldehydes 3-phosphate dehydrogenase (GAPDH), 3-phosphoglycerate kinase, glucose isomerase, phosphofructokinase, and pyruvate kinase (3,4) and that the interaction may be electrostatic in nature (3).
(1980) with an ATP-regenerating system consisting of phosphoenolpyruvate and pyruvate kinase. CK catalyzes the phosphorylation of glycocyamine, albeit at a much lower rate than creatine.
Activities of two enzymes, citrate synthase (CS) and pyruvate kinase (PK), were determined by methods given in Choi et al.

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